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標題: Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion
作者: Chen, S.Y.
Chen, H.C.
關鍵字: receptor tyrosine kinase;c-met;ferm domain;oncogenic rearrangement;terminal domain;protein;gab1;phosphorylation;activation;motility
Project: Molecular and Cellular Biology
期刊/報告no:: Molecular and Cellular Biology, Volume 26, Issue 13, Page(s) 5155-5167.
Focal adhesion kinase (FAK) has been implicated to be a point of convergence of integrin and growth factor signaling pathways. Here we report that FAK directly interacts with the hepatocyte growth factor receptor c-Met. Phosphorylation of c-Met at Tyr-1349 and, to a lesser extent, Tyr-1356 is required for its interaction with the band 4.1 and ezrin/radixin/moesin homology domain (FERM domain) of FAK. The F2 subdomain of the FAK FERM domain alone is sufficient for Met binding, in which a patch of basic residues ((216)KAKTLRK(222)) are critical for the interaction. Met-FAK interaction leads to FAK activation and subsequent contribution to hepatocyte growth factor-induced cell motility and cell invasion. Our results provide evidence that constitutive Met-FAK interaction may be a critical determinant for tumor cells to acquire invasive potential.
ISSN: 0270-7306
DOI: 10.1128/mcb.02186-05
Appears in Collections:生命科學院

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